Low molecular weight cadmium—and copper-binding proteins from rat kidneys

1980 ◽  
Vol 2 (2) ◽  
pp. 137-148 ◽  
Author(s):  
Andrzej J. Żelazowski ◽  
Jadwiga A. Szymańska
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Low Molecular Weight ◽  
Copper Binding ◽  
Rat Kidneys ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins in the plasma of winter flounder (Pseudopleuronectes americanus)

1980 ◽  
Vol 58 (4) ◽  
pp. 609-613 ◽  
Author(s):  
P. E. Fletcher ◽  
G. L. Fletcher
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Egg Yolk ◽  
Winter Flounder ◽  
Zinc Binding ◽  
Copper Binding ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins were isolated from the plasma of winter flounder using gel filtration chromatography. A single copper-binding protein fraction of molecular weight 170 000 was isolated from the plasma of both sexes.In male and female flounder over 95% of the plasma zinc was associated with a zinc-binding protein(s) with a molecular weight of 76 000. In male flounder the remaining zinc appeared to be bound to a protein(s) of molecular weight 186 000. In female flounder the remaining 5% of the zinc was associated with two zinc-binding fractions with apparent molecular weights of 186 000 and 340 000 – 370 000.Extracts of plasma vitellogenin and egg yolk proteins revealed significant quantities of zinc and copper. It is hypothesized that the female specific zinc-binding protein (340 000 – 370 000) was vitellogenin.

High molecular weight zinc- and copper-binding proteins in the liver of the rat; Effect of centrifugation

1987 ◽  
Vol 135 (2) ◽  
pp. 129-132
Author(s):  
J.B. Dielhof, ◽  
J.G. Van Der Enden, ◽  
TH.M.W. Stolk ◽  
C.J.A. Van Den Hamer,
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Binding Proteins ◽  
Copper Binding ◽  
Copper Binding Proteins

Isolation of copper-binding proteins from activated sludge culture

2001 ◽  
Vol 44 (2-3) ◽  
pp. 453-459 ◽  
Author(s):  
K. Fukushi ◽  
S. Kato ◽  
T. Antsuki ◽  
T. Omura
Keyword(s):  
Molecular Weight ◽  
Activated Sludge ◽  
Metal Uptake ◽  
Binding Proteins ◽  
Growth Media ◽  
Copper Binding ◽  
Molecular Weights ◽  
Binding Capability ◽  
Copper Binding Proteins

Six copper-binding microbial proteins were isolated from activated sludge cultures grown on media containing copper at various concentrations. Molecular weights among isolated proteins were ranged from 1.3k to 174k dalton. Isolated proteins were compared for their copper binding capabilities. Proteins isolated from cultures grown in the presence of copper in the growth media exhibited higher copper binding capabilities than those isolated from the culture grown in the absence of copper. The highest metal uptake of 61.23 (mol copper/mol protein) was observed by a protein isolated from a culture grown with copper at a concentration of 0.25 mM. This isolated protein (CBP2) had a molecular weight of 24k dalton. Other protein exhibited copper binding capability of 4.8-32.5 (mol copper/mol protein).

scholarly journals A study of the copper-binding proteins in liver and kidney tissue of neonatal normal and mottled mutant mice

1979 ◽  
Vol 183 (3) ◽  
pp. 721-730 ◽  
Author(s):  
A E Port ◽  
D M Hunt
Keyword(s):  
Molecular Weight ◽  
Glutamic Acid ◽  
Binding Proteins ◽  
Kidney Tissue ◽  
Weight Fraction ◽  
Exchange Chromatography ◽  
Low Molecular Weight ◽  
Copper Binding ◽  
Liver And Kidney ◽  
Cysteine Content

The Cu2+-binding proteins from liver and kidney tissue of 7–8-day-old brindled (Mobr) mice and their normal littermates were compared. (1) Separation over Bio-Gel P-10 showed that the differences in the Cu2+ content of mutant tissues were largely associated with a low-molecular-weight protein fraction (mol.wt. 14 500). (2) Further purification of this low-molecular-weight fraction by anion-exchange chromatography revealed four subfractions. The Cu2+ content of each subfraction reflected the Cu2+ status of the tissue of origin; the Cu2+ contents of the mutant kidney subfractions were elevated and those of the mutant liver were depressed compared with normal. In contrast, the protein contents of the subfractions were less variable and did not reflect the differing Cu2+ contents. (3) Amino acid analysis of the four subfractions from CuCl2-treated mutant and normal animals revealed clos similarities. The proteins showed high glycine, glutamic acid, serine, alanine and lysine contents and a rather variable cysteine content. Differences were apparent in the normal liver subfractions, which showed a higher cysteine content and lower glutamic acid content than did either the mutant liver or normal and mutant kidney subfractions. These observations, together with the recorded presence of aromatic amino acids, indicated that these proteins are not thioneins.

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

Rapid induction of copper-binding proteins in the gills of metal exposed mussels

1980 ◽  
Vol 67 (2) ◽  
pp. 215-218 ◽  
Author(s):  
A. Viarengo ◽  
M. Pertica ◽  
G. Mancinelli ◽  
G. Zanicchi ◽  
M. Orunesu
Keyword(s):  
Binding Proteins ◽  
Copper Binding ◽  
Rapid Induction ◽  
Copper Binding Proteins

scholarly journals Influence of hypersulfated and low molecular weight heparins on ischemia/reperfusion: injury and allograft rejection in rat kidneys

2007 ◽  
Vol 20 (6) ◽  
pp. 542-549 ◽  
Author(s):  
Uwe Gottmann ◽  
Astrid Mueller-Falcke ◽  
Peter Schnuelle ◽  
Rainer Birck ◽  
Volker Nickeleit ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Reperfusion Injury ◽  
Allograft Rejection ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Low Molecular Weight ◽  
Low Molecular Weight Heparins ◽  
Rat Kidneys

Stability and Folding of Copper-Binding Proteins

2010 ◽  
pp. 61-80
Author(s):  
Irina Pozdnyakova ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Binding Proteins ◽  
Copper Binding ◽  
Copper Binding Proteins
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